Cathepsins are proteases that normally localized in lysosomes of almost all mammalian cells, but under certain conditions they can be secreted from the cell. Cathepsins are classified based on their functions and presence of active site such as cathepsin B, D, K, V, F etc.
Monoclonal Anti-Cathepsin K (mouse IgG2b isotype) is derived from the hybridoma CK124-1H6 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with recombinant human cathepsin K.
Specificity
The antibody does not cross react with the closely related lysosomal cysteine proteases cathepsins L, B, H, S, V and W.
Immunogen
recombinant human cathepsin K. The antibody epitope resides within the peptide sequence RGYREIPEGNEKAL that corresponds to amino acids 222-235.
Application
Monoclonal Anti-Cathepsin K antibody produced in mouse has been used in western blotting and enzyme linked immunosorbent assay (ELISA).
Biochem/physiol Actions
Cathepsin is involved in various functions such as intracellular degradation of exogenous and endogenous proteins, activation of enzyme precursors, and tumor invasion and metastasis. Among all the types, cathepsins K (Ctsk) is highly expressed in osteoclasts that plays a crucial role in bone remodeling and resorption. Cathepsin K protein was found in primary breast carcinoma and prostate cancer where it performs in the invasive process of prostate cancers, thyroid carcinoma, lung adenocarcinoma and breast carcinoma. Its deficency causes pycnodysostosis, a rare bone dysplasia with an osteopetrotic-like phenotype.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Clinica chimica acta; international journal of clinical chemistry, 237(1-2), 67-78 (1995-06-15)
In the metastatic process, proteolytic enzymes play an important role in mediating passage of the malignant cell through the cell membrane. The cathepsins are ubiquitous lysosomal proteases and are classified both functionally and according to their active site. Cathepsin D
The Journal of biological chemistry, 271(21), 12511-12516 (1996-05-24)
Random high throughput sequencing of a human osteoclast cDNA library was employed to identify novel osteoclast-expressed genes. Of the 5475 ESTs obtained, approximately 4% encoded cathepsin K, a novel cysteine protease homologous to cathepsins S and L; ESTs for other
Cysteine cathepsins (11 in humans) are mostly located in the acidic compartments of cells. They have been known for decades to be involved in intracellular protein degradation as housekeeping proteases. However, the discovery of new cathepsins, including cathepsins K, V
Expert opinion on investigational drugs, 18(5), 585-600 (2009-04-25)
Cathepsin K is a highly potent collagenase and the predominant papain-like cysteine protease expressed in osteoclasts. Cathepsin K deficiencies in humans and mice have underlined the central role of this protease in bone resorption and, thus, have rendered the enzyme
The Journal of biological chemistry, 273(48), 32347-32352 (1998-11-21)
Type I collagen fibers account for 90% of the organic matrix of bone. The degradation of this collagen is a major event during bone resorption, but its mechanism is unknown. A series of data obtained in biological models strongly suggests
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